دورية أكاديمية

Novel Peptides with Dual Properties for Treating Pseudomonas aeruginosa Keratitis: Antibacterial and Corneal Wound Healing

التفاصيل البيبلوغرافية
العنوان: Novel Peptides with Dual Properties for Treating Pseudomonas aeruginosa Keratitis: Antibacterial and Corneal Wound Healing
المؤلفون: Floriana Cappiello, Sudhir Verma, Xiao Lin, Isabel Y. Moreno, Bruno Casciaro, Debarun Dutta, Alison M. McDermott, Mark Willcox, Vivien J. Coulson-Thomas, Maria Luisa Mangoni
المصدر: Biomolecules, Vol 13, Iss 7, p 1028 (2023)
بيانات النشر: MDPI AG, 2023.
سنة النشر: 2023
المجموعة: LCC:Microbiology
مصطلحات موضوعية: antimicrobial peptides, corneal wound healing, Pseudomonas aeruginosa, keratitis, corneal infections, antimicrobial resistance, Microbiology, QR1-502
الوصف: The corneal epithelium is a layer in the anterior part of eye that contributes to light refraction onto the retina and to the ocular immune defense. Although an intact corneal epithelium is an excellent barrier against microbial pathogens and injuries, corneal abrasions can lead to devastating eye infections. Among them, Pseudomonas aeruginosa-associated keratitis often results in severe deterioration of the corneal tissue and even blindness. Hence, the discovery of new drugs able not only to eradicate ocular infections, which are often resistant to antibiotics, but also to elicit corneal wound repair is highly demanded. Recently, we demonstrated the potent antipseudomonal activity of two peptides, Esc(1-21) and its diastereomer Esc(1-21)-1c. In this study, by means of a mouse model of P. aeruginosa keratitis and an in vivo corneal debridement wound, we discovered the efficacy of these peptides, particularly Esc(1-21)-1c, to cure keratitis and to promote corneal wound healing. This latter property was also supported by in vitro cell scratch and ELISA assays. Overall, the current study highlights Esc peptides as novel ophthalmic agents for treating corneal infection and injury, being able to display a dual function, antimicrobial and wound healing, rarely identified in a single peptide at the same micromolar concentration range.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 2218-273X
العلاقة: https://www.mdpi.com/2218-273X/13/7/1028Test; https://doaj.org/toc/2218-273XTest
DOI: 10.3390/biom13071028
الوصول الحر: https://doaj.org/article/5752f9125184411c8b607b687c48f271Test
رقم الانضمام: edsdoj.5752f9125184411c8b607b687c48f271
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:2218273X
DOI:10.3390/biom13071028